Evidence of proteolipid domain formation in an inner mitochondrial membrane mimicking model

M. CHENIOUR; J. BREWER; L. A. BAGATOLLI; 0. MARCILLAT; T. GRANJON

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2017 vol. 1861 p. 969 - 969

0304-4165

h4>BACKGROUND: Mitochondrial creatine kinase (mtCK) is highly abundant in mitochondria; its quantity is equimolecular to the Adenylic Nucleotide Translocator and represents 1% of the mitochondrial proteins. It is a multitask protein localized in the mitochondria intermembrane space where it binds to the specific cardiolipin (CL) phospholipid. If mtCK was initially thought to be exclusively implicated in energy transfer between mitochondria and cytosol through a mechanism referred to as the phosphocreatine shuttle, several recent studies suggested an additional role in maintaining mitochondria membrane structure.METHODS: To further characterized mtCK binding process we used multiphoton excitation fluorescence microscopy coupled with Giant Unilamellar Vesicles (GUV) and laurdan as fluorescence probe.RESULTS: We gathered structural and dynamical information on the molecular events occurring during the binding of mtCK to the mitochondria inner membr